› 2i03

X-ray diffraction
2.4Å resolution

Function and Biology Details

Reaction catalysed: 
Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151015 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dipeptidyl peptidase 4 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 726 amino acids
Theoretical weight: 84.25 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P27487 (Residues: 39-764; Coverage: 95%)
Gene names: ADCP2, CD26, DPP4
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand AXD 1 x AXD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P21
Unit cell:
a: 120.252Å b: 126.994Å c: 127.257Å
α: 90° β: 96.56° γ: 90°
R-values:
R R work R free
0.179 0.179 0.245
Expression system: Spodoptera frugiperda

Quick links

Citations

5 review citations

The lipophilic bullet hits the targets: medicinal chemistry of adamantane derivatives.
Wanka et al. (2013)
4 more

6 mentions without citation

SUMOylation modulates the function of Aurora-B kinase.
Fernández-Miranda et al. (2010)
5 more